Forum for Science, Industry and Business

Sponsored by:     3M 
Search our Site:

 

Bucket with two ears catches DNA

16.05.2003


Dutch PhD student Cathelijne Kloks has discovered that the so-called Cold Shock domain of the human YB-1 protein looks like a bucket with two extra ears. These ears lead the DNA to the binding site on the protein and keep it there.



Kloks investigated the structure and function of one of the three domains of the human protein YB-1. This protein plays an important role in the production of new proteins. The central domain, the so-called Cold Shock domain, ensures the binding of the protein to the DNA in the process.

The researcher from the University of Nijmegen discovered that the domain looks like a bucket with a handle and two extra ears. The ears attach to the DNA and push it to the binding site on the YB-1. This binding site was found to be located precisely in between the two ears. This means that the ears can hold the DNA firmly in place whilst it is being bound to the protein. The function of the handle is not yet clear.


Kloks dissolved the YB-1 protein and then studied the solution using NMR measurements. She used the NMR signals to draw up a distances table, which indicated the distance between the nuclei of atoms in the protein. With this information she then calculated the structure of the Cold Shock domain.

Furthermore, Kloks determined the strength of the binding to the DNA. The Cold Shock domain alone formed weak bonds to the DNA. This did not agree with previously made measurements of the binding strength of the complete YB-1 protein. The domain also exhibited little preference with respect to where it binds to the DNA, although previous experiments had shown that the Cold Shock domain binds more strongly to areas of DNA containing a lot of cytosine and thymine. Kloks concluded that the protein’s considerable binding strength and preference could only be clarified by including its other two domains.

In the cell YB-1 forms the link between the transcription of the DNA and the subsequent production of a new protein. YB-1 consists of three different domains. These are compact parts which can fold independently without using other parts of the protein.

The Cold Shock domain derives its name from its function in bacteria. In bacterial proteins the domain ensures that the bacteria resume growth, following a period of arrested growth due to a sudden drop in temperature.

For further information please contact Cathelijne Kloks (Department of Medicinal Chemistry, Organon) tel. +31 (0)412 662461 e-mail: c.kloks@organon.com. The doctoral thesis will be defended on 26 May 2003. Ms Kloks’’ supervisor is Prof. C.W. Hilbers (University of Nijmegen).

Nalinie Moerlie | alfa
Further information:
http://www.nwo.nl

More articles from Life Sciences:

nachricht Fish recognize their prey by electric colors
13.11.2018 | Rheinische Friedrich-Wilhelms-Universität Bonn

nachricht The dawn of a new era for genebanks - molecular characterisation of an entire genebank collection
13.11.2018 | Leibniz-Institut für Pflanzengenetik und Kulturpflanzenforschung

All articles from Life Sciences >>>

The most recent press releases about innovation >>>

Die letzten 5 Focus-News des innovations-reports im Überblick:

Im Focus: A Chip with Blood Vessels

Biochips have been developed at TU Wien (Vienna), on which tissue can be produced and examined. This allows supplying the tissue with different substances in a very controlled way.

Cultivating human cells in the Petri dish is not a big challenge today. Producing artificial tissue, however, permeated by fine blood vessels, is a much more...

Im Focus: A Leap Into Quantum Technology

Faster and secure data communication: This is the goal of a new joint project involving physicists from the University of Würzburg. The German Federal Ministry of Education and Research funds the project with 14.8 million euro.

In our digital world data security and secure communication are becoming more and more important. Quantum communication is a promising approach to achieve...

Im Focus: Research icebreaker Polarstern begins the Antarctic season

What does it look like below the ice shelf of the calved massive iceberg A68?

On Saturday, 10 November 2018, the research icebreaker Polarstern will leave its homeport of Bremerhaven, bound for Cape Town, South Africa.

Im Focus: Penn engineers develop ultrathin, ultralight 'nanocardboard'

When choosing materials to make something, trade-offs need to be made between a host of properties, such as thickness, stiffness and weight. Depending on the application in question, finding just the right balance is the difference between success and failure

Now, a team of Penn Engineers has demonstrated a new material they call "nanocardboard," an ultrathin equivalent of corrugated paper cardboard. A square...

Im Focus: Coping with errors in the quantum age

Physicists at ETH Zurich demonstrate how errors that occur during the manipulation of quantum system can be monitored and corrected on the fly

The field of quantum computation has seen tremendous progress in recent years. Bit by bit, quantum devices start to challenge conventional computers, at least...

All Focus news of the innovation-report >>>

Anzeige

Anzeige

VideoLinks
Industry & Economy
Event News

“3rd Conference on Laser Polishing – LaP 2018” Attracts International Experts and Users

09.11.2018 | Event News

On the brain’s ability to find the right direction

06.11.2018 | Event News

European Space Talks: Weltraumschrott – eine Gefahr für die Gesellschaft?

23.10.2018 | Event News

 
Latest News

The dawn of a new era for genebanks - molecular characterisation of an entire genebank collection

13.11.2018 | Life Sciences

Fish recognize their prey by electric colors

13.11.2018 | Life Sciences

Ultrasound Connects

13.11.2018 | Awards Funding

VideoLinks
Science & Research
Overview of more VideoLinks >>>